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P13498 (CY24A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 148. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cytochrome b-245 light chain
Alternative name(s):
Cytochrome b(558) alpha chain
Cytochrome b558 subunit alpha
Neutrophil cytochrome b 22 kDa polypeptide
Superoxide-generating NADPH oxidase light chain subunit
p22 phagocyte B-cytochrome
p22-phox
Short name=p22phox
Gene names
Name:CYBA
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length195 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Critical component of the membrane-bound oxidase of phagocytes that generates superoxide. Associates with NOX3 to form a functional NADPH oxidase constitutively generating superoxide. Ref.10

Subunit structure

Composed of a heavy chain (beta) and a light chain (alpha). Component of an NADPH oxidase complex composed of a heterodimer formed by the membrane proteins CYBA and CYBB and the cytosolic subunits NCF1, NCF2 and NCF4. Interacts with NCF1 (via SH3 domain). Interacts with SH3PXD2A By similarity. Interacts with DUOX1, DUOX2 and TPO. Interacts with NOX3 and NOX4. Interacts with calprotectin (S100A8/9). Ref.7 Ref.9 Ref.11 Ref.13 Ref.14

Subcellular location

Cell membrane Ref.8 Ref.13.

Post-translational modification

The heme prosthetic group could be coordinated with residues of the light chain, the heavy chain, or both, and it is possible that more than one heme is present per cytochrome b-245.

Phosphorylation at Thr-147 enhances NADPH oxidase activity by promoting p47phox binding By similarity.

Involvement in disease

Granulomatous disease, chronic, cytochrome-b-negative, autosomal recessive (ARCGD) [MIM:233690]: A disorder characterized by the inability of neutrophils and phagocytes to kill microbes that they have ingested. Patients suffer from life-threatening bacterial/fungal infections.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.5 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22

Sequence similarities

Belongs to the p22phox family.

Ontologies

Keywords
   Biological processElectron transport
Transport
   Cellular componentCell membrane
Membrane
   Coding sequence diversityPolymorphism
   DiseaseChronic granulomatous disease
Disease mutation
   LigandHeme
Iron
Metal-binding
NADP
   Molecular functionOxidoreductase
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processantigen processing and presentation of exogenous peptide antigen via MHC class I

Traceable author statement. Source: Reactome

antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent

Traceable author statement. Source: Reactome

antigen processing and presentation of peptide antigen via MHC class I

Traceable author statement. Source: Reactome

cellular response to amino acid stimulus

Inferred from electronic annotation. Source: Ensembl

cellular response to gamma radiation

Inferred from electronic annotation. Source: Ensembl

cellular response to glucose stimulus

Inferred from electronic annotation. Source: Ensembl

cellular response to mechanical stimulus

Inferred from electronic annotation. Source: Ensembl

cellular response to organic cyclic compound

Inferred from electronic annotation. Source: Ensembl

cellular response to tumor necrosis factor

Inferred from electronic annotation. Source: Ensembl

cytochrome complex assembly

Inferred from direct assay PubMed 7938008. Source: BHF-UCL

hydrogen peroxide biosynthetic process

Inferred from sequence or structural similarity. Source: BHF-UCL

inflammatory response

Inferred from mutant phenotype Ref.5. Source: BHF-UCL

innate immune response

Inferred from mutant phenotype Ref.5. Source: BHF-UCL

interaction with host

Traceable author statement. Source: Reactome

negative regulation of glomerular filtration by angiotensin

Inferred from electronic annotation. Source: Ensembl

oxidation-reduction process

Inferred from mutant phenotype Ref.16Ref.5. Source: BHF-UCL

phagosome maturation

Traceable author statement. Source: Reactome

positive regulation of cell growth

Inferred from electronic annotation. Source: Ensembl

positive regulation of endothelial cell proliferation

Inferred from electronic annotation. Source: Ensembl

respiratory burst

Inferred from mutant phenotype Ref.5. Source: BHF-UCL

response to drug

Inferred from electronic annotation. Source: Ensembl

response to interleukin-1

Inferred from electronic annotation. Source: Ensembl

response to nutrient levels

Inferred from electronic annotation. Source: Ensembl

smooth muscle hypertrophy

Inferred from sequence or structural similarity. Source: BHF-UCL

superoxide anion generation

Inferred from mutant phenotype Ref.5. Source: BHF-UCL

superoxide metabolic process

Inferred from mutant phenotype Ref.16Ref.5. Source: BHF-UCL

   Cellular_componentGolgi apparatus

Inferred from electronic annotation. Source: Ensembl

NADPH oxidase complex

Inferred from direct assay PubMed 3305576. Source: BHF-UCL

apical plasma membrane

Inferred from electronic annotation. Source: Ensembl

dendrite

Inferred from electronic annotation. Source: Ensembl

mitochondrion

Inferred from electronic annotation. Source: Ensembl

neuronal cell body

Inferred from electronic annotation. Source: Ensembl

phagocytic vesicle membrane

Traceable author statement. Source: Reactome

secretory granule

Traceable author statement PubMed 12005167. Source: BHF-UCL

   Molecular_functionSH3 domain binding

Inferred from physical interaction PubMed 7938008. Source: BHF-UCL

electron carrier activity

Traceable author statement Ref.5. Source: UniProtKB

heme binding

Inferred from electronic annotation. Source: InterPro

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction Ref.14PubMed 16460309PubMed 17126813PubMed 17803994PubMed 23957209. Source: IntAct

protein heterodimerization activity

Inferred from physical interaction PubMed 12042318. Source: BHF-UCL

superoxide-generating NADPH oxidase activity

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.1
Chain2 – 195194Cytochrome b-245 light chain
PRO_0000144907

Regions

Intramembrane91 – 12737
Compositional bias133 – 18957Pro-rich

Sites

Metal binding941Iron (heme axial ligand) Potential

Amino acid modifications

Modified residue1471Phosphothreonine Ref.12
Modified residue1681Phosphoserine By similarity

Natural variations

Natural variant241G → R in ARCGD. Ref.19 Ref.20 Ref.21
Corresponds to variant rs28941476 [ dbSNP | Ensembl ].
VAR_012755
Natural variant251G → V in ARCGD. Ref.19
Corresponds to variant rs179363891 [ dbSNP | Ensembl ].
VAR_060576
Natural variant521L → P in ARCGD. Ref.19
Corresponds to variant rs179363890 [ dbSNP | Ensembl ].
VAR_060577
Natural variant531E → V in ARCGD. Ref.17
Corresponds to variant rs179363893 [ dbSNP | Ensembl ].
VAR_060578
Natural variant721Y → H. Ref.1 Ref.6 Ref.23
Corresponds to variant rs4673 [ dbSNP | Ensembl ].
VAR_005122
Natural variant901R → Q in ARCGD. Ref.15
VAR_005123
Natural variant901R → W in ARCGD. Ref.19
Corresponds to variant rs179363892 [ dbSNP | Ensembl ].
VAR_060579
Natural variant941H → R in ARCGD. Ref.15
VAR_005124
Natural variant1181S → R in ARCGD. Ref.5 Ref.19
Corresponds to variant rs104894514 [ dbSNP | Ensembl ].
VAR_005125
Natural variant1241A → V in ARCGD. Ref.21
Corresponds to variant rs179363894 [ dbSNP | Ensembl ].
VAR_060580
Natural variant1251A → T in ARCGD. Ref.22
VAR_060581
Natural variant1561P → Q in ARCGD. Ref.16 Ref.18
VAR_005126
Natural variant1711E → G. Ref.23
Corresponds to variant rs72667005 [ dbSNP | Ensembl ].
VAR_060582
Natural variant1741V → A. Ref.1 Ref.2 Ref.4 Ref.6 Ref.23
Corresponds to variant rs1049254 [ dbSNP | Ensembl ].
VAR_054801
Natural variant1931E → D. Ref.23
VAR_060583

Experimental info

Mutagenesis1571P → Q: Loss of interaction with NOXO1. Ref.7

Secondary structure

... 195
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P13498 [UniParc].

Last modified November 2, 2010. Version 3.
Checksum: 428427AD19398240

FASTA19521,013
        10         20         30         40         50         60 
MGQIEWAMWA NEQALASGLI LITGGIVATA GRFTQWYFGA YSIVAGVFVC LLEYPRGKRK 

        70         80         90        100        110        120 
KGSTMERWGQ KYMTAVVKLF GPFTRNYYVR AVLHLLLSVP AGFLLATILG TACLAIASGI 

       130        140        150        160        170        180 
YLLAAVRGEQ WTPIEPKPRE RPQIGGTIKQ PPSNPPPRPP AEARKKPSEE EAAVAAGGPP 

       190 
GGPQVNPIPV TDEVV 

« Hide

References

« Hide 'large scale' references
[1]"Primary structure and unique expression of the 22-kilodalton light chain of human neutrophil cytochrome b."
Parkos C.A., Dinauer M.C., Walker L.E., Allen R.A., Jesaitis A.J., Orkin S.H.
Proc. Natl. Acad. Sci. U.S.A. 85:3319-3323(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 2-26, VARIANTS HIS-72 AND ALA-174.
[2]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ALA-174.
[3]"The sequence and analysis of duplication-rich human chromosome 16."
Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J. expand/collapse author list , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ALA-174.
Tissue: Brain.
[5]"Human neutrophil cytochrome b light chain (p22-phox). Gene structure, chromosomal location, and mutations in cytochrome-negative autosomal recessive chronic granulomatous disease."
Dinauer M.C., Pierce E.A., Bruns G.A.P., Curnutte J.T., Orkin S.H.
J. Clin. Invest. 86:1729-1737(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 12-123, VARIANT ARCGD ARG-118.
[6]"Characterization of two monoclonal antibodies against cytochrome b558 of human neutrophils."
Verhoeven A.J., Bolscher B.G., Meerhof L.J., van Zwieten R., Keijer J., Weening R.S., Roos D.
Blood 73:1686-1694(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 51-195, VARIANTS HIS-72 AND ALA-174.
[7]"Novel human homologues of p47phox and p67phox participate in activation of superoxide-producing NADPH oxidases."
Takeya R., Ueno N., Kami K., Taura M., Kohjima M., Izaki T., Nunoi H., Sumimoto H.
J. Biol. Chem. 278:25234-25246(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NOXO1, MUTAGENESIS OF PRO-157.
[8]"Site-specific inhibitors of NADPH oxidase activity and structural probes of flavocytochrome b: characterization of six monoclonal antibodies to the p22phox subunit."
Taylor R.M., Burritt J.B., Baniulis D., Foubert T.R., Lord C.I., Dinauer M.C., Parkos C.A., Jesaitis A.J.
J. Immunol. 173:7349-7357(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, MEMBRANE TOPOLOGY.
[9]"Identification of a novel partner of duox: EFP1, a thioredoxin-related protein."
Wang D., De Deken X., Milenkovic M., Song Y., Pirson I., Dumont J.E., Miot F.
J. Biol. Chem. 280:3096-3103(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DUOX1; DUOX2 AND TPO.
[10]"The NADPH oxidase Nox3 constitutively produces superoxide in a p22phox-dependent manner: its regulation by oxidase organizers and activators."
Ueno N., Takeya R., Miyano K., Kikuchi H., Sumimoto H.
J. Biol. Chem. 280:23328-23339(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[11]"Functional analysis of Nox4 reveals unique characteristics compared to other NADPH oxidases."
Martyn K.D., Frederick L.M., von Loehneysen K., Dinauer M.C., Knaus U.G.
Cell. Signal. 18:69-82(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NOX4.
[12]"Phosphorylation of p22phox on threonine 147 enhances NADPH oxidase activity by promoting p47phox binding."
Lewis E.M., Sergeant S., Ledford B., Stull N., Dinauer M.C., McPhail L.C.
J. Biol. Chem. 285:2959-2967(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT THR-147.
[13]"Molecular interface of S100A8 with cytochrome b and NADPH oxidase activation."
Berthier S., Nguyen M.V., Baillet A., Hograindleur M.A., Paclet M.H., Polack B., Morel F.
PLoS ONE 7:E40277-E40277(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH CALPROTECTIN.
[14]"NMR solution structure of the tandem Src homology 3 domains of p47phox complexed with a p22phox-derived proline-rich peptide."
Ogura K., Nobuhisa I., Yuzawa S., Takeya R., Torikai S., Saikawa K., Sumimoto H., Inagaki F.
J. Biol. Chem. 281:3660-3668(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 149-167 IN COMPLEX WITH NCF1, INTERACTION WITH NCF1.
[15]"Cytochrome b558-negative, autosomal recessive chronic granulomatous disease: two new mutations in the cytochrome b558 light chain of the NADPH oxidase (p22-phox)."
de Boer M., de Klein A., Hossle J.-P., Seger R., Corbeel L., Weening R.S., Roos D.
Am. J. Hum. Genet. 51:1127-1135(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ARCGD GLN-90 AND ARG-94.
[16]"Point mutation in the cytoplasmic domain of the neutrophil p22-phox cytochrome b subunit is associated with a nonfunctional NADPH oxidase and chronic granulomatous disease."
Dinauer M.C., Pierce E.A., Erickson R.W., Muhlebach T.J., Messner H., Orkin S.H., Seger R.A., Curnutte J.T.
Proc. Natl. Acad. Sci. U.S.A. 88:11231-11235(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ARCGD GLN-156.
[17]"Identification of allele-specific p22-phox mutations in a compound heterozygous patient with chronic granulomatous disease by mismatch PCR and restriction enzyme analysis."
Hossle J.-P., de Boer M., Seger R.A., Roos D.
Hum. Genet. 93:437-442(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ARCGD VAL-53.
[18]"156Pro-->Gln substitution in the light chain of cytochrome b558 of the human NADPH oxidase (p22-phox) leads to defective translocation of the cytosolic proteins p47-phox and p67-phox."
Leusen J.H., Bolscher B.G., Hilarius P.M., Weening R.S., Kaulfersch W., Seger R.A., Roos D., Verhoeven A.J.
J. Exp. Med. 180:2329-2334(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF VARIANT ARCGD GLN-156.
[19]"Molecular analysis of 9 new families with chronic granulomatous disease caused by mutations in CYBA, the gene encoding p22(phox)."
Rae J., Noack D., Heyworth P.G., Ellis B.A., Curnutte J.T., Cross A.R.
Blood 96:1106-1112(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ARCGD ARG-24; VAL-25; PRO-52; TRP-90 AND ARG-118.
[20]"Genetic studies of three Japanese patients with p22-phox-deficient chronic granulomatous disease: detection of a possible common mutant CYBA allele in Japan and a genotype-phenotype correlation in these patients."
Yamada M., Ariga T., Kawamura N., Ohtsu M., Imajoh-Ohmi S., Ohshika E., Tatsuzawa O., Kobayashi K., Sakiyama Y.
Br. J. Haematol. 108:511-517(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ARCGD ARG-24.
[21]"Statistical and mutational analysis of chronic granulomatous disease in Japan with special reference to gp91-phox and p22-phox deficiency."
Ishibashi F., Nunoi H., Endo F., Matsuda I., Kanegasaki S.
Hum. Genet. 106:473-481(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ARCGD ARG-24 AND VAL-124.
[22]"Characterization of six novel mutations in CYBA: the gene causing autosomal recessive chronic granulomatous disease."
Teimourian S., Zomorodian E., Badalzadeh M., Pouya A., Kannengiesser C., Mansouri D., Cheraghi T., Parvaneh N.
Br. J. Haematol. 141:848-851(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ARCGD THR-125.
[23]"Three common polymorphisms in the CYBA gene form a haplotype associated with decreased ROS generation."
Bedard K., Attar H., Bonnefont J., Jaquet V., Borel C., Plastre O., Stasia M.-J., Antonarakis S.E., Krause K.-H.
Hum. Mutat. 30:1123-1133(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HIS-72; GLY-171; ALA-174 AND ASP-193.
+Additional computationally mapped references.

Web resources

CYBAbase

CYBA mutation db

SHMPD

The Singapore human mutation and polymorphism database

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M21186 mRNA. Translation: AAA90925.1.
BT006861 mRNA. Translation: AAP35507.1.
AC116552 Genomic DNA. No translation available.
BC006465 mRNA. Translation: AAH06465.1.
AH002664 Genomic DNA. Translation: AAA52134.1.
CCDSCCDS32504.1.
PIRA28201.
RefSeqNP_000092.2. NM_000101.3.
UniGeneHs.513803.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1WLPNMR-A149-168[»]
ProteinModelPortalP13498.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107915. 8 interactions.
DIPDIP-37650N.
IntActP13498. 7 interactions.
MINTMINT-5209680.
STRING9606.ENSP00000261623.

Protein family/group databases

TCDB5.B.1.1.1. the phagocyte (gp91(phox)) nadph oxidase family.

PTM databases

PhosphoSiteP13498.

Polymorphism databases

DMDM311033459.

Proteomic databases

MaxQBP13498.
PaxDbP13498.
PeptideAtlasP13498.
PRIDEP13498.

Protocols and materials databases

DNASU1535.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000261623; ENSP00000261623; ENSG00000051523.
GeneID1535.
KEGGhsa:1535.
UCSCuc002flb.4. human.

Organism-specific databases

CTD1535.
GeneCardsGC16M088709.
GeneReviewsCYBA.
H-InvDBHIX0013335.
HGNCHGNC:2577. CYBA.
HPACAB009492.
MIM233690. phenotype.
608508. gene.
neXtProtNX_P13498.
Orphanet379. Chronic granulomatous disease.
PharmGKBPA27075.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG39609.
HOGENOMHOG000001585.
HOVERGENHBG051278.
InParanoidP13498.
KOK08009.
OMAKIEWAMW.
PhylomeDBP13498.
TreeFamTF328901.

Enzyme and pathway databases

ReactomeREACT_116125. Disease.
REACT_6900. Immune System.

Gene expression databases

ArrayExpressP13498.
BgeeP13498.
CleanExHS_CYBA.
GenevestigatorP13498.

Family and domain databases

InterProIPR007732. Cyt_b558_asu.
[Graphical view]
PANTHERPTHR15168. PTHR15168. 1 hit.
PfamPF05038. Cytochrom_B558a. 1 hit.
[Graphical view]
PIRSFPIRSF019635. Cytochr_b558a. 1 hit.
ProtoNetSearch...

Other

ChiTaRSCYBA. human.
EvolutionaryTraceP13498.
GenomeRNAi1535.
NextBio6349.
PROP13498.
SOURCESearch...

Entry information

Entry nameCY24A_HUMAN
AccessionPrimary (citable) accession number: P13498
Secondary accession number(s): Q14090, Q9BR72
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: November 2, 2010
Last modified: July 9, 2014
This is version 148 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 16

Human chromosome 16: entries, gene names and cross-references to MIM